BMRB Entry 16320
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16320
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution structure of an archaeal protein SSO6904 from hyperthermophilic Sulfolobus solfataricus PubMed: 19768683
Deposition date: 2009-05-28 Original release date: 2009-10-14
Authors: Feng, Yingang; Yao, Hongwei; Wang, Jinfeng
Citation: Feng, Yingang; Yao, Hongwei; Wang, Jinfeng. "Solution structure and calcium binding of protein SSO6904 from the hyperthermophilic archaeon Sulfolobus solfataricus." Proteins 78, 474-479 (2010).
Assembly members:
SSO6904, polymer, 99 residues, 11913.870 Da.
Natural source: Common Name: Sulfolobus solfataricus Taxonomy ID: 2287 Superkingdom: Archaea Kingdom: not available Genus/species: Sulfolobus solfataricus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
SSO6904: MSILEDPEFVKLRQFKGKVN
FNLVMQILDEIELDLRGSDN
IKTSIIYVYSSHLDEIRKNK
EFYDMIAEILQRYYKKIGIE
NVNQLILTTIKLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 433 |
| 15N chemical shifts | 96 |
| 1H chemical shifts | 703 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SSO6904 | 1 |
Entities:
Entity 1, SSO6904 99 residues - 11913.870 Da.
| 1 | MET | SER | ILE | LEU | GLU | ASP | PRO | GLU | PHE | VAL | ||||
| 2 | LYS | LEU | ARG | GLN | PHE | LYS | GLY | LYS | VAL | ASN | ||||
| 3 | PHE | ASN | LEU | VAL | MET | GLN | ILE | LEU | ASP | GLU | ||||
| 4 | ILE | GLU | LEU | ASP | LEU | ARG | GLY | SER | ASP | ASN | ||||
| 5 | ILE | LYS | THR | SER | ILE | ILE | TYR | VAL | TYR | SER | ||||
| 6 | SER | HIS | LEU | ASP | GLU | ILE | ARG | LYS | ASN | LYS | ||||
| 7 | GLU | PHE | TYR | ASP | MET | ILE | ALA | GLU | ILE | LEU | ||||
| 8 | GLN | ARG | TYR | TYR | LYS | LYS | ILE | GLY | ILE | GLU | ||||
| 9 | ASN | VAL | ASN | GLN | LEU | ILE | LEU | THR | THR | ILE | ||||
| 10 | LYS | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: SS6904, [U-13C; U-15N], 1 – 1.5 mM; potassium phosphate 50 mM; potassium chloride 100 mM; D2O, [U-99.8% 2H], 10%; DSS 0.02 % w/v; sodium azide 0.02 % w/v; arginine 50 mM; glutamic acid 50 mM; H2O 90%
sample_conditions_1: ionic strength: 0.15 M; pH: 7.2; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHANH | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
xwinnmr, Bruker Biospin - collection
FELIX, Accelrys Software Inc. - chemical shift assignment, data analysis, peak picking, processing
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution
NMR spectrometers:
- Bruker DMX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts